Expression of these deletion mutants was demonstrated by WB and immunofluorescence staining using anti-GFP antibody (Fig 5C).
The molecular lesion for one of these mutants was demonstrated to be a mutation in CYP79A1, the first enzyme in dhurrin production.
The higher content of fatty acids in the wild type strain compared with the Δ9 desaturase mutants was demonstrated by both GC-FID and LC-MS analysis, yet it was not detected by Oil Red-O staining.
Compared with RRASWT, aberrant binding behaviour of the two RRAS mutants was demonstrated, with RRASG39dup exhibiting an increased binding affinity towards PIK3CA, RAF1, PLCE1 and RASSF5, and RRASV55M to RALGDS.
Furthermore, wild-type and Ser587Ala HA–SIK2, but not the Ser358Ala mutant, was demonstrated to directly bind 14-3-3 14-3-3 14-3-3-stinulated rat adipoCLtes, as detected using co-immunoprecipitation and far-Western blotting.
The RNA and DNA sequences used in the experiment of Figure 4D are shown in Table 2.> Residual activity of the D998N R508A N509A Pol α mutant was demonstrated by the primer extension assay, as described; the protein concentration in the assay was varied over a range of concentrations up to 10 μM.
Consistent with the negative modulatory role of the C-terminal region on SOS1 function [Corbalan-Garcia et al., 1998; Wang et al., 1995], the SOS1 mutant was demonstrated to localize at the plasma membrane constitutively and sustain the activation of RAS MAPK signaling, linking the gingival overgrowth to enhanced SOS1-mediated signal flow through RAS [Jang et al., 2007].
Mutant T-allele carriers were demonstrated to have a higher risk for hearing impairment than homozygotic carriers of the wild-type allele in several models that adjust for different combinations of confounding variables.
Furthermore, the roles of CsFAD2 in PUFA synthesis were demonstrated by mutant analysis and by antisense gene expression in camelina seed.
Following meta-analysis, associations were demonstrated for mutant TP53, ERCC1 rs11615 and XRCC1 rs25487.
